大肠杆菌的zntA基因编码一种锌（II）转运P型ATP酶。
The zntA gene of Escherichia coli encodes a Zn(II)-translocating P-type ATPase.
作者信息
Rensing C, Mitra B, Rosen B P
机构信息
Department of Biochemistry and Molecular Biology, Wayne State University School of Medicine, 540 East Canfield Avenue, Detroit, MI 48201, USA.
出版信息
Proc Natl Acad Sci U S A. 1997 Dec 23;94(26):14326-31. doi: 10.1073/pnas.94.26.14326.
The first Zn(II)-translocating P-type ATPase has been identified as the product of o732, a potential gene identified in the sequencing of the Escherichia coli genome. This gene, termed zntA, was disrupted by insertion of a kanamycin gene through homologous recombination. The mutant strain exhibited hypersensitivity to zinc and cadmium salts but not salts of other metals, suggesting a role in zinc homeostasis in E. coli. Everted membrane vesicles from a wild-type strain accumulated 65Zn(II) and 109Cd(II) by using ATP as an energy source. Transport was sensitive to vanadate, an inhibitor of P-type ATPases. Membrane vesicles from the zntA::kan strain did not accumulate those metal ions. Both the sensitive phenotype and transport defect of the mutant were complemented by expression of zntA on a plasmid.
首个锌（II）转运P型ATP酶已被确定为o732的产物，o732是在大肠杆菌基因组测序中鉴定出的一个潜在基因。这个名为zntA的基因通过同源重组插入卡那霉素基因而被破坏。突变菌株对锌盐和镉盐表现出超敏反应，但对其他金属盐则无此反应，这表明它在大肠杆菌的锌稳态中发挥作用。野生型菌株的外翻膜囊泡利用ATP作为能量来源积累65锌（II）和109镉（II）。转运对钒酸盐敏感，钒酸盐是P型ATP酶的抑制剂。来自zntA::kan菌株的膜囊泡不积累那些金属离子。突变体的敏感表型和转运缺陷都通过在质粒上表达zntA得到互补。
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